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P17519 (P1_PLRV1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein P1
Alternative name(s):
69.7 kDa protein
Genome-linked protein precursor
Protein ORF1

Cleaved into the following 2 chains:

  1. Serine protease
    EC=3.4.21.-
  2. VPg/P1-C25
Gene names
ORF Names:ORF1
OrganismPotato leafroll virus (strain Potato/Scotland/strain 1/1984) (PLrV) [Reference proteome]
Taxonomic identifier12046 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageLuteoviridaePolerovirus
Virus hostSolanum tuberosum (Potato) [TaxID: 4113]

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Precursor from which the VPg molecule is probably released at the onset of the RNA synthesis. Essential for virus replication.

Subcellular location

Protein P1: Membrane; Multi-pass membrane protein Potential.

Domain

The C-terminus part of protein P1 and VPg/P1-C25 displays RNA-binding properties.

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins. The protease probably cleaves itself and releases the VPg protein. The VPg protein is probably further cleaved in its C-terminus. Ref.3

Sequence similarities

Belongs to the peptidase S39B family.

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]
Isoform Protein P1 (identifier: P17519-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by conventional translation.
Isoform RNA-directed RNA polymerase (identifier: P17520-1)

The sequence of this isoform can be found in the external entry P17520.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshifting between codons 487 and 488.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 639619Protein P1
PRO_0000222396
Chain205 – 399195Serine protease Potential
PRO_0000390899
Chain400 – 639240VPg/P1-C25 Potential
PRO_0000390900

Regions

Transmembrane121 – 14121Helical; Potential
Transmembrane144 – 16421Helical; Potential
Transmembrane172 – 19221Helical; Potential
Compositional bias68 – 714Poly-Pro

Sites

Active site2551 Probable
Active site2861 Probable
Active site3541 Probable
Site204 – 2052Cleavage; by viral serine protease Potential
Site399 – 4002Cleavage; by viral serine protease Probable

Experimental info

Mutagenesis2551H → L: Complete loss of viral genomic or subgenomic RNA production. Ref.5
Mutagenesis2861D → A: Complete loss of viral genomic or subgenomic RNA production. Ref.5
Mutagenesis3541S → A: Complete loss of viral genomic or subgenomic RNA production. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform Protein P1 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: AFCF2FB393BEE097

FASTA63969,629
        10         20         30         40         50         60 
MNRFTAYAAL FFMFSLCSTA KEAGFLHPAF NFRGTSTMSA SSGDYSAAPT PLYKSWALPS 

        70         80         90        100        110        120 
SLNLTTQPPP PLTDRSYYEL VQALTSKMRL DCQTVGDMTW RHLSEMLFAS WNSVKEVSLK 

       130        140        150        160        170        180 
AASVTLWAII NIWFGLYWTL ARLITLFLWT FSIEALCLIL LGCITSLIYK GALSLSEHLP 

       190        200        210        220        230        240 
VFLFMSPLKI IWRAAFSKRN YKNERAVEGY KGFSVPQKPP KSAVIELQHE NGSHLGYANC 

       250        260        270        280        290        300 
IRLYSGENAL VTAEHCLEGA FATSLKTGNR IPMSTFFPIF KSARNDISIL VGPPNWEGLL 

       310        320        330        340        350        360 
SVKGAHFITA DKIGKGPASF YTLEKGEWMC HSATIDGAHH QFVSVLCNTG PGYSGTGFWS 

       370        380        390        400        410        420 
SKNLLGVLKG FPLEEECNYN VMSVIPSIPG ITSPNYVFES TAVKGRVFSD EAVKELEREA 

       430        440        450        460        470        480 
SEAVKKLARF KSLTDKNWAD DYDSDEDYGL EREAATNAPA EKTAQTNSAE KTAPSTSAEK 

       490        500        510        520        530        540 
TALTNKPLNG QAAPSAKTNG NSDIPDAATS APPMDKMVEQ IITAMVGRIN LSEIEEKIVS 

       550        560        570        580        590        600 
RVSQKALQKP KQKKRGRRGG KNKQNSLPPT STQSTSGAPK KEAAPQASGS AGTSRATTTP 

       610        620        630 
APEAKPSGGK NSAKFTPSWR IKQQDSAGQK PDLKLNSKA 

« Hide

Isoform RNA-directed RNA polymerase [UniParc].

See P17520.

References

[1]"Nucleotide sequence of potato leafroll luteovirus RNA."
Mayo M.A., Robinson D.J., Jolly C.A., Hyman L.
J. Gen. Virol. 70:1037-1051(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Ribosomal frameshifting in plants: a novel signal directs the -1 frameshift in the synthesis of the putative viral replicase of potato leafroll luteovirus."
Prufer D., Tacke E., Schmitz J., Kull B., Kaufmann A., Rohde W.
EMBO J. 11:1111-1117(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: RIBOSOMAL FRAMESHIFTING.
[3]"The genome-linked protein of potato leafroll virus is located downstream of the putative protease domain of the ORF1 product."
van der Wilk F., Verbeek M., Dullemans A.M., van den Heuvel J.F.J.M.
Virology 234:300-303(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, IDENTIFICATION OF VPG, PROTEIN SEQUENCE OF 400-431.
[4]"Immunological analysis of potato leafroll luteovirus (PLRV) P1 expression identifies a 25 kDa RNA-binding protein derived via P1 processing."
Prufer D., Kawchuk L., Monecke M., Nowok S., Fischer R., Rohde W.
Nucleic Acids Res. 27:421-425(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING.
[5]"Mutational analysis of the proteinase function of Potato leafroll virus."
Sadowy E., Juszczuk M., David C., Gronenborn B., Hulanicka M.D.
J. Gen. Virol. 82:1517-1527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES OF SERINE PROTEASE, MUTAGENESIS OF HIS-255; ASP-286 AND SER-354.
Strain: Isolate Polish.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00530 Genomic RNA. Translation: BAA00417.1.
PIRWMVQ70. JA0118.
RefSeqNP_056747.1. NC_001747.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1493894.

Family and domain databases

InterProIPR018019. Luteovirus_Orf2.
IPR000382. Peptidase_S39B_luteovirus.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF02122. Peptidase_S39. 1 hit.
[Graphical view]
PRINTSPR00913. LVIRUSORF2.
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
ProtoNetSearch...

Entry information

Entry nameP1_PLRV1
AccessionPrimary (citable) accession number: P17519
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 3, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families